5txk

X-ray diffraction
1.84Å resolution

CRYSTAL STRUCTURE OF USP35 C450S IN COMPLEX WITH UBIQUITIN

Released:

Function and Biology Details

Reaction catalysed:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-143291 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase 35 Chain: A
Molecule details ›
Chain: A
Length: 372 amino acids
Theoretical weight: 41.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P2H5 (Residues: 423-944; Coverage: 37%)
Gene names: KIAA1372, USP34, USP35
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-003
Spacegroup: P43212
Unit cell:
a: 104.235Å b: 104.235Å c: 106.381Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.183
Expression system: Escherichia coli